Protein-O-mannosyltransferases in virulence and development

Protein-O-mannosyltransferases (Pmt proteins) catalyse the addition of mannose to serine or threonine residues of secretory proteins. This modification was described first for yeast and later for other fungi, mammals, insects and recently also for bacteria. O-mannosylation depends on specific isofor...

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Published inCellular and molecular life sciences : CMLS Vol. 65; no. 4; pp. 528 - 544
Main Authors Lengeler, K. B, Tielker, D, Ernst, J. F
Format Journal Article
LanguageEnglish
Published Basel Basel : SP Birkhäuser Verlag Basel 01.02.2008
Birkhäuser-Verlag
Springer Nature B.V
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Summary:Protein-O-mannosyltransferases (Pmt proteins) catalyse the addition of mannose to serine or threonine residues of secretory proteins. This modification was described first for yeast and later for other fungi, mammals, insects and recently also for bacteria. O-mannosylation depends on specific isoforms of the three Pmt1, 2 and 4 subfamilies. In fungi, O-mannosylation determines the structure and integrity of cell walls, as well as cellular differentiation and virulence. O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans and of the bacterial pathogen Mycobacterium tuberculosis contributes significantly to virulence. In mammals and insects, Pmt proteins are essential for cellular differentiation and development, while lack of Pmt activity causes Walker-Warburg syndrome (muscular dystrophy) in humans. The susceptibility of human cells to certain viruses may also depend on O-mannosyl chains. This review focuses on the various roles of Pmt proteins in cellular differentiation, development and virulence.
Bibliography:http://dx.doi.org/10.1007/s00018-007-7409-z
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ISSN:1420-682X
1420-9071
DOI:10.1007/s00018-007-7409-z